CATH Classification
| Level | CATH Code | Description |
|---|---|---|
|
1 | Mainly Alpha |
|
1.10 | Orthogonal Bundle |
|
1.10.8 | Helicase, Ruva Protein; domain 3 |
|
1.10.8.10 | DNA helicase RuvA subunit, C-terminal domain |
Domain Context
CATH Clusters
| Superfamily | DNA helicase RuvA subunit, C-terminal domain |
| Functional Family |
Enzyme Information
| 2.3.2.23 |
E2 ubiquitin-conjugating enzyme.
based on mapping to UniProt P61086
S-ubiquitinyl-[E1 ubiquitin-activating enzyme]-L-cysteine + [E2 ubiquitin-conjugating enzyme]-L-cysteine = [E1 ubiquitin-activating enzyme]-L-cysteine + S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L- cysteine.
-!- The E2 ubiquitin-conjugating enzyme acquires the activated ubquitin from the E1 ubiquitin-activating enzyme (EC 6.2.1.45) and binds it via a transthioesterification reaction to itself. -!- In the human enzyme the catalytic center is located at Cys-87 where ubiquitin is bound via its C-terminal glycine in a thioester linkage. -!- Formerly EC 6.3.2.19.
|
UniProtKB Entries (1)
| P61086 |
UBE2K_HUMAN
Homo sapiens
Ubiquitin-conjugating enzyme E2 K
|
PDB Structure
| PDB | 6IF1 |
| External Links | |
| Method | X-RAY DIFFRACTION |
| Organism | |
| Primary Citation |
Crystal structure of the Ube2K/E2-25K and K48-linked di-ubiquitin complex provides structural insight into the mechanism of K48-specific ubiquitin chain synthesis.
Biochem. Biophys. Res. Commun.
|
